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The Crystal Structure of a Biological Insulated Transmembrane Molecular Wire

A growing number of bacteria are recognized to conduct electrons across their cell envelope, and yet molecular details of the mechanisms supporting this process remain unknown. Here, we report the atomic structure of an outer membrane spanning protein complex, MtrAB, that is representative of a prot...

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Detalles Bibliográficos
Autores principales: Edwards, Marcus J., White, Gaye F., Butt, Julea N., Richardson, David J., Clarke, Thomas A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cell Press 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7198977/
https://www.ncbi.nlm.nih.gov/pubmed/32289252
http://dx.doi.org/10.1016/j.cell.2020.03.032
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author Edwards, Marcus J.
White, Gaye F.
Butt, Julea N.
Richardson, David J.
Clarke, Thomas A.
author_facet Edwards, Marcus J.
White, Gaye F.
Butt, Julea N.
Richardson, David J.
Clarke, Thomas A.
author_sort Edwards, Marcus J.
collection PubMed
description A growing number of bacteria are recognized to conduct electrons across their cell envelope, and yet molecular details of the mechanisms supporting this process remain unknown. Here, we report the atomic structure of an outer membrane spanning protein complex, MtrAB, that is representative of a protein family known to transport electrons between the interior and exterior environments of phylogenetically and metabolically diverse microorganisms. The structure is revealed as a naturally insulated biomolecular wire possessing a 10-heme cytochrome, MtrA, insulated from the membrane lipidic environment by embedding within a 26 strand β-barrel formed by MtrB. MtrAB forms an intimate connection with an extracellular 10-heme cytochrome, MtrC, which presents its hemes across a large surface area for electrical contact with extracellular redox partners, including transition metals and electrodes.
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spelling pubmed-71989772020-05-05 The Crystal Structure of a Biological Insulated Transmembrane Molecular Wire Edwards, Marcus J. White, Gaye F. Butt, Julea N. Richardson, David J. Clarke, Thomas A. Cell Article A growing number of bacteria are recognized to conduct electrons across their cell envelope, and yet molecular details of the mechanisms supporting this process remain unknown. Here, we report the atomic structure of an outer membrane spanning protein complex, MtrAB, that is representative of a protein family known to transport electrons between the interior and exterior environments of phylogenetically and metabolically diverse microorganisms. The structure is revealed as a naturally insulated biomolecular wire possessing a 10-heme cytochrome, MtrA, insulated from the membrane lipidic environment by embedding within a 26 strand β-barrel formed by MtrB. MtrAB forms an intimate connection with an extracellular 10-heme cytochrome, MtrC, which presents its hemes across a large surface area for electrical contact with extracellular redox partners, including transition metals and electrodes. Cell Press 2020-04-30 /pmc/articles/PMC7198977/ /pubmed/32289252 http://dx.doi.org/10.1016/j.cell.2020.03.032 Text en Crown Copyright © 2020 Published by Elsevier Inc. http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Edwards, Marcus J.
White, Gaye F.
Butt, Julea N.
Richardson, David J.
Clarke, Thomas A.
The Crystal Structure of a Biological Insulated Transmembrane Molecular Wire
title The Crystal Structure of a Biological Insulated Transmembrane Molecular Wire
title_full The Crystal Structure of a Biological Insulated Transmembrane Molecular Wire
title_fullStr The Crystal Structure of a Biological Insulated Transmembrane Molecular Wire
title_full_unstemmed The Crystal Structure of a Biological Insulated Transmembrane Molecular Wire
title_short The Crystal Structure of a Biological Insulated Transmembrane Molecular Wire
title_sort crystal structure of a biological insulated transmembrane molecular wire
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7198977/
https://www.ncbi.nlm.nih.gov/pubmed/32289252
http://dx.doi.org/10.1016/j.cell.2020.03.032
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